1990
DOI: 10.1007/bf00633832
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Expression of foreign epitopes in P-fimbriae ofEscherichia coli

Abstract: Hypervariable regions (HRs) of the major subunit of F11 fimbriae were exploited for insertion of foreign epitopes. Two insertion vectors were created that contain a unique cloning site in HR1 or HR4 respectively. Several oligonucleotides, coding for antigenic determinants derived from different pathogens, were cloned in both insertion vectors. Hybrid fimbrial subunits were generally shown to be assembled in fimbriae when the length of the inserted peptide did not exceed 14 amino acids. The inserted peptides ap… Show more

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Cited by 22 publications
(7 citation statements)
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“…This construction resulted in the insertion of 27 additional amino acid residues into FasA. A third TGEV epitope could not be added to this site (data not shown), suggesting that successful fimbria export and assembly constrain the length of an inserted segment, as proposed previously (4,7,73,76). Moreover, as observed with the CS31A fimbriae (7,46), the addition of the TGEV A epitope resulted both in decreased fimbria production and in significant cleavage of chimeric subunits.…”
Section: Discussionmentioning
confidence: 62%
“…This construction resulted in the insertion of 27 additional amino acid residues into FasA. A third TGEV epitope could not be added to this site (data not shown), suggesting that successful fimbria export and assembly constrain the length of an inserted segment, as proposed previously (4,7,73,76). Moreover, as observed with the CS31A fimbriae (7,46), the addition of the TGEV A epitope resulted both in decreased fimbria production and in significant cleavage of chimeric subunits.…”
Section: Discussionmentioning
confidence: 62%
“…Several bacterial surface proteins have been successfully fused and found to express foreign proteins. These include PhoE [3], LamB [11], peptidoglycan-associated lipoprotein [15], flagellin [24,27], P-fimbriae [18,40] and TraT [37].…”
Section: Discussionmentioning
confidence: 99%
“…Fimbriae are adhesive surface organelles that enable bacteria to target and colonize specific host tissues. A large variety of fimbrial proteins have been used for surface display, including the FimA and FimH proteins of type 1 fimbriae [34,58], the FelA subunit of type P fimbriae [59] and the major structural subunit of type 4 fimbriae, to name a few [60]. Fimbriae proteins are present at extremely high numbers on the cell surface, which make them attractive for display purposes; however, the major structural proteins of various fimbriae can only accommodate relatively small inserts (10–30 amino acids) without disturbing the organelle structure and surface‐ display efficiency [61].…”
Section: Surface‐display Systems For Bacteriamentioning
confidence: 99%